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Article: Inhibition of alcohol dehydrogenase by bismuth

TitleInhibition of alcohol dehydrogenase by bismuth
Authors
Issue Date2004
PublisherElsevier Inc. The Journal's web site is located at http://www.elsevier.com/locate/jinorgbio
Citation
Journal Of Inorganic Biochemistry, 2004, v. 98 n. 8, p. 1331-1337 How to Cite?
AbstractBismuth compounds have been widely used for the treatment of ulcers and Helicobacter pylori infection, and enzyme inhibition was thought to be crucial for bismuth anti-microbial activity. We have investigated the interaction of colloidal bismuth subcitrate (CBS) with alcohol dehydrogenase and our results demonstrate that bismuth can effectively inhibit the enzyme. Kinetic analysis revealed that CBS acted as a non-competitive inhibitor of yeast alcohol dehydrogenase. Both UV-vis and fluorescence data show that interaction of CBS with the enzyme exhibits biphasic processes. Bismuth can replace only half of Zn(II) from the enzyme (i.e., about one Zn(II) per monomer). Surprisingly, binding of CBS also induces the enzyme dissociation from its native form, tetramer into dimers. The inhibition of Bi(III) on the enzyme is probably due to its direct interference with the zinc sites. This study is likely to provide an insight into the mechanism of action of bismuth drugs. © 2004 Elsevier Inc. All rights reserved.
Persistent Identifierhttp://hdl.handle.net/10722/168001
ISSN
2015 Impact Factor: 3.205
2015 SCImago Journal Rankings: 0.983
ISI Accession Number ID
References

 

DC FieldValueLanguage
dc.contributor.authorJin, Len_US
dc.contributor.authorSzeto, KYen_US
dc.contributor.authorZhang, Len_US
dc.contributor.authorDu, Wen_US
dc.contributor.authorSun, Hen_US
dc.date.accessioned2012-10-08T03:13:58Z-
dc.date.available2012-10-08T03:13:58Z-
dc.date.issued2004en_US
dc.identifier.citationJournal Of Inorganic Biochemistry, 2004, v. 98 n. 8, p. 1331-1337en_US
dc.identifier.issn0162-0134en_US
dc.identifier.urihttp://hdl.handle.net/10722/168001-
dc.description.abstractBismuth compounds have been widely used for the treatment of ulcers and Helicobacter pylori infection, and enzyme inhibition was thought to be crucial for bismuth anti-microbial activity. We have investigated the interaction of colloidal bismuth subcitrate (CBS) with alcohol dehydrogenase and our results demonstrate that bismuth can effectively inhibit the enzyme. Kinetic analysis revealed that CBS acted as a non-competitive inhibitor of yeast alcohol dehydrogenase. Both UV-vis and fluorescence data show that interaction of CBS with the enzyme exhibits biphasic processes. Bismuth can replace only half of Zn(II) from the enzyme (i.e., about one Zn(II) per monomer). Surprisingly, binding of CBS also induces the enzyme dissociation from its native form, tetramer into dimers. The inhibition of Bi(III) on the enzyme is probably due to its direct interference with the zinc sites. This study is likely to provide an insight into the mechanism of action of bismuth drugs. © 2004 Elsevier Inc. All rights reserved.en_US
dc.languageengen_US
dc.publisherElsevier Inc. The Journal's web site is located at http://www.elsevier.com/locate/jinorgbioen_US
dc.relation.ispartofJournal of Inorganic Biochemistryen_US
dc.subject.meshAlcohol Dehydrogenase - Antagonists & Inhibitors - Genetics - Metabolismen_US
dc.subject.meshAmino Acid Sequenceen_US
dc.subject.meshAnimalsen_US
dc.subject.meshAnti-Infective Agents - Chemistry - Metabolismen_US
dc.subject.meshBismuth - Chemistry - Metabolismen_US
dc.subject.meshEnzyme Stabilityen_US
dc.subject.meshMolecular Sequence Dataen_US
dc.subject.meshOrganometallic Compounds - Chemistry - Metabolismen_US
dc.subject.meshSaccharomyces Cerevisiae - Genetics - Metabolismen_US
dc.subject.meshSaccharomyces Cerevisiae Proteins - Antagonists & Inhibitors - Genetics - Metabolismen_US
dc.subject.meshSequence Alignmenten_US
dc.subject.meshZinc - Chemistryen_US
dc.titleInhibition of alcohol dehydrogenase by bismuthen_US
dc.typeArticleen_US
dc.identifier.emailSun, H:hsun@hkucc.hku.hken_US
dc.identifier.authoritySun, H=rp00777en_US
dc.description.naturelink_to_subscribed_fulltexten_US
dc.identifier.doi10.1016/j.jinorgbio.2004.03.016en_US
dc.identifier.pmid15271509-
dc.identifier.scopuseid_2-s2.0-3242677993en_US
dc.identifier.hkuros104234-
dc.relation.referenceshttp://www.scopus.com/mlt/select.url?eid=2-s2.0-3242677993&selection=ref&src=s&origin=recordpageen_US
dc.identifier.volume98en_US
dc.identifier.issue8en_US
dc.identifier.spage1331en_US
dc.identifier.epage1337en_US
dc.identifier.isiWOS:000223383600010-
dc.publisher.placeUnited Statesen_US
dc.identifier.scopusauthoridJin, L=7403328801en_US
dc.identifier.scopusauthoridSzeto, KY=7006866001en_US
dc.identifier.scopusauthoridZhang, L=8085225300en_US
dc.identifier.scopusauthoridDu, W=7202953617en_US
dc.identifier.scopusauthoridSun, H=7404827446en_US
dc.identifier.citeulike3813820-

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